Purification of human neutrophil NADPH oxidase cytochrome b-558 and association with Rap 1A.

Purification of human neutrophil NADPH oxidase cytochrome b-558 and association with Rap 1A.
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人中性粒细胞 NADPH 氧化酶细胞色素 b-558 的纯化及其与 Rap 1A 的关联。

DOI:
10.1016/s0076-6879(95)55050-x
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发表时间:
1995
影响因子:
--
通讯作者:
Jesaitis,AJ
Jesaitis,AJ
中科院分区:
生物学4区
文献类型:
--
作者:
Quinn,MT;Parkos,CA;Jesaitis,AJ

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获得足够数量的高纯度吞噬细胞细胞色素b-558是对这一重要的NADPH氧化酶组分进行许多生化和免疫学分析所必需的,只有通过对高纯度细胞色素b的分析,才能阐明亚基的组成,并克隆和测序小亚基(p22-Phox)。此外,通过对纯化的细胞色素b的分析,还发现了小的GTP结合蛋白Rap1a与细胞色素b-558的结合。本方法为细胞色素b以及细胞色素b-Rap1a复合体的纯化提供了一种简便、高效、重复性高的方法。纯化细胞色素b和细胞色素b-Rap1a复合体的能力也将有助于进一步分析这种新的质膜氧化还原蛋白的结构,以及它与低分子GTP结合蛋白在吞噬细胞NADPH氧化酶的结构和调节中的作用。
The availability of sufficient quantities of highly purified phagocyte cytochrome b-558 has been necessary for many of the biochemical and immunological analyses of this important NADPH oxidase component, and it was only through the analysis of highly purified cytochrome b that the subunit composition was elucidated and the small subunit (p22-phox) was cloned and sequenced. In addition, the association of the small GTP-binding protein Rap1A with cytochrome b-558 was discovered through the analysis of purified cytochrome b. The procedures described here provide an easy, efficient, and highly reproducible method for the purification of cytochrome b as well as cytochrome b-Rap1A complexes. The ability to purify cytochrome b and cytochrome b-Rap1A complexes will also allow further analysis of the structure of this novel plasma membrane redox protein and the role of its association with low molecular weight GTP-binding proteins in the structure and regulation of the phagocyte NADPH oxidase.
DOI: 10.1016/0005-2728(88)90140-5
发表时间: 1988
期刊: Biochimica et biophysica acta
影响因子: --
作者:
Charles A. Parkos;Rodger A. Allen;Charles G. Cochrane;A. J. Jesaitis
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DOI: 10.1172/jci114898
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发表时间: 1988
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